Channel gate! Tension, leak and disclosure

Channel gate! Tension, leak and disclosure
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DOI:
10.1016/s0969-2126(99)80061-6
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发表时间:
1999-05-01
期刊:
影响因子:
5.7
通讯作者:
Kung, C
Kung, C
中科院分区:
生物学2区
文献类型:
--
作者:
Batiza, AF;Rayment, I;Kung, C

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细菌MSCL的晶体结构显示了这种同膜通道蛋白是如何在静止时被紧紧闭合以防止泄漏的。通过推断,该结构还显示了脂质双层中的拉伸力如何导致通道打开。我们现在有了一幅具体的图景,说明了刺激是如何“关闭”离子通道的。
The crystal structure of a bacterial MscL shows how this homopentameric channel protein is held tightly shut to prevent leakage whilst at rest. By inference, the structure also shows how a stretch force in the lipid bilayer causes the channel to open. We now have a concrete picture as to how a stimulus 'gates' an ion channel.